2JHK
Structure of globular heads of M-ficolin complexed with N-acetyl-D- glucosamine
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 39 |
Details | Region: {"description":"A domain; contributes to trimerization"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 88 |
Details | Region: {"description":"B domain; contributes to trimerization"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Region: {"description":"P domain","evidences":[{"source":"PubMed","id":"17148457","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17148457","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17897951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20032467","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2D39","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WNP","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17897951","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Mediates specificity for sialic acids","evidences":[{"source":"PubMed","id":"17897951","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20032467","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Site: {"description":"Mediates specificity for sialic acids","evidences":[{"source":"PubMed","id":"17897951","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |